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The amino acid sequence of adiantum capillus-veneres photochrome has been deduced form the nucleuotide suquence of a cDNA clone (pFP1) which was initially identified by hybridization to a pea type I poytochrome cDAN clone. Ninety percent of nucleotide sequence has been done but ten percent still remained unidentified. Homology is high at the N-terminal region, especially around the chromophore attachment site, but lower at C-terminal region. Comparison among the amino acid sequences of type I, II, III of Arabidopsis and Adiantum phytochrome did not show any special resembrance of fern phytochrome to any of the three types of Arabidopsis. Overall, the fern phytochrome is rather similar to higher plant phytochrome as far as hydropathy profile is concerned, suggesting that the phytochrome molecule is not trans-membranous protein but water soluble, although fern phytochrome has been shownTo raise anti-fern phytochrome antibodies, 3 polypeptides made of 15 amino acids around hydrophilic regions deduced from nucleuotide sequence of pFP1 were synthesized. Fusion protein of this clone was also produced as an antigen. Production of monoclonal antibodies of this fern phytochrome is now underway.